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Borrelia burgdorferi Binds Fibronectin through a Tandem -ߚipper, a Common Mechanism of Fibronectin Binding in Staphylococci, Streptococci, and Spirochetes

Raibaud, S., Schwarz-Linek, U., Kim, J., Jenkins, H.T., Baines, E.R., Gurusiddappa, S., Höök, M. and Potts, J.R. (2005) Borrelia burgdorferi Binds Fibronectin through a Tandem -ߚipper, a Common Mechanism of Fibronectin Binding in Staphylococci, Streptococci, and Spirochetes. Journal Of Biological Chemistry, 280 (19). pp. 18803-18809. ISSN 0021-9258

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Abstract

BBK32 is a fibronectin-binding protein from the Lyme disease-causing spirochete Borrelia burgdorferi. In this study, we show that BBK32 shares sequence similarity with fibronectin module-binding motifs previously identified in proteins from Streptococcus pyogenes and Staphylococcus aureus. Nuclear magnetic resonance spectroscopy and isothermal titration calorimetry are used to confirm the binding sites of BBK32 peptides within the N-terminal domain of fibronectin and to measure the affinities of the interactions. Comparison of chemical shift perturbations in fibronectin F1 modules on binding of peptides from BBK32, FnBPA from S. aureus, and SfbI from S. pyogenes provides further evidence for a shared mechanism of binding. Despite the different locations of the bacterial attachment sites in BBK32 compared with SfbI from S. pyogenes and FnBPA from S. aureus, an antiparallel orientation is observed for binding of the N-terminal domain of fibronectin to each of the pathogens. Thus, these phylogenetically and morphologically distinct bacterial pathogens have similar mechanisms for binding to human fibronectin.

Item Type: Article
Institution: The University of York
Academic Units: The University of York > Chemistry (York)
Depositing User: York RAE Import
Date Deposited: 23 Apr 2009 14:35
Last Modified: 23 Apr 2009 14:35
Published Version: http://dx.doi.org/10.1074/jbc.M501731200
Status: Published
Publisher: The American Society for Biochemistry and Molecular Biology
Identification Number: 10.1074/jbc.M501731200
URI: http://eprints.whiterose.ac.uk/id/eprint/6598

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